3PF1
E. coli FadL Asp348Ala mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-06-01 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.97981 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.880, 145.970, 151.240 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.480 - 2.700 |
| R-factor | 0.2135 |
| Rwork | 0.210 |
| R-free | 0.27270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1t16 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.133 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.5_2)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.000 | 2.950 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.118 | 0.514 |
| Number of reflections | 39050 | |
| <I/σ(I)> | 11.4 | 4 |
| Completeness [%] | 98.4 | 98.4 |
| Redundancy | 4.6 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 295 | 15-17% PEG 4K 0.2M KCl, protein dialysed in 10mM NaOAc 50mM NaCl, 10% glycerol 0.4%C8E4, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
